Open AccessThe heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap
Author(s) -
Piper Peter W.
Publication year - 1995
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1995.tb07925.x
Subject(s) - ethanol , heat shock protein , yeast , atpase , chemistry , membrane , hsp70 , biophysics , shock (circulatory) , membrane permeability , biochemistry , membrane protein , microbiology and biotechnology , enzyme , biology , medicine , gene
Abstract Sublethal heat and ethanol exposure induce essentially identical stress responses in yeast. These responses are characterized by the induction of heat shock proteins, proteins requiring a temperature above about 35 °C or ethanol levels above a threshold level of 4–6% (v/v) for strong induction. One induced protein, Hsp104, contributes to both thermotolerance and ethanol tolerance, while others are anti‐oxidant enzymes. Heat and ethanol stress cause similar changes to plasma membrane protein composition, reducing the levels of plasma membrane H + ‐ATPase protein and inducing the plasma membrane‐associated Hsp30. Both stresses also stimulate the activity of the fraction of H + ‐ATPase remaining in the plasma membrane. The resulting enhancement to catalysed proton efflux from the cell represents a considerable energy demand, yet may help to counteract the adverse effects for homeostasis of the increased membrane permeability that results from stress.